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BioMed Research International
Volume 2013 (2013), Article ID 326914, 8 pages
Interplay between Peptide Bond Geometrical Parameters in Nonglobular Structural Contexts
1Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
2Seconda Università di Napoli, Via Vivaldi 43, 81100 Caserta, Italy
3Division of Molecular Biosciences, Imperial College South Kensington Campus, London SW7 2AZ, UK
Received 10 September 2013; Accepted 29 November 2013
Academic Editor: Kei Yura
Copyright © 2013 Luciana Esposito et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Fig. S1 reports the distribution of the resolution of membrane protein and amyloid-like peptide crystal structures considered in the present study.
Fig. S2 reports the overall Ramachandran plot for residues belonging to the transmembrane regions of membrane proteins.
Fig. S3 reports the distribution of N-Cα-C values for residues in α-helices, β-sheets and 3-10 helices in the selected dataset of membrane protein structures.
Fig. S4 reports some examples in which the tight interdigitation leads to a significant deformation of the N-Cα-C angle in amyloid-like peptides.
Fig S5 reports the dependence of θC pyramidalization on ψ for residues of the collagen-like peptide (Pro-Pro-Gly)9.